› 2hqt

X-ray diffraction
1.9Å resolution

Crystal structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA aminoacylation and nuclear export cofactor Arc1p reveal a novel function for an old fold

Released:
DOI: 10.2210/pdb2hqt/pdb
PDB entry 2hqt coloured by chain, front view.
PDB entry 2hqt coloured by chain, side view.
PDB entry 2hqt coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA-aminoacylation and nuclear-export cofactor Arc1p reveal a novel function for an old fold.
Simader H, Hothorn M, Suck D
Acta Crystallogr D Biol Crystallogr 62 1510-9 (2006)
PMID: 17139087

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155498 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA-aminoacylation cofactor ARC1 Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T
Length: 124 amino acids
Theoretical weight: 14.2 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P46672 (Residues: 1-122; Coverage: 32%)
Gene names: ARC1, G3085, G4P1, YGL105W
Structure domains: Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2

Ligands and Environments

1 bound ligand:
Ligand SO4 10 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1, SLS BEAMLINE X06SA
Spacegroup: C2
Unit cell:
a: 222.317Å b: 89.463Å c: 126.792Å
α: 90° β: 99.39° γ: 90°
R-values:
R R work R free
0.212 0.209 0.262
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Aminoacyl-tRNA synthetase complexes: molecular multitasking revealed.
Hausmann et al. (2008)
1 more

1 mention without citation

Protein-protein docking benchmark version 3.0.
Hwang et al. (2008)